SitesBLAST
Comparing AO356_16420 FitnessBrowser__pseudo5_N2C3_1:AO356_16420 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P07821 Iron(3+)-hydroxamate import ATP-binding protein FhuC; Ferric hydroxamate uptake protein C; Ferrichrome transport ATP-binding protein FhuC; Iron(III)-hydroxamate import ATP-binding protein FhuC; EC 7.2.2.16 from Escherichia coli (strain K12) (see 2 papers)
38% identity, 94% coverage: 10:257/263 of query aligns to 9:261/265 of P07821
- K50 (= K51) mutation to Q: Lack of activity.
- D172 (= D173) mutation to E: Lack of activity.
- E173 (= E174) mutation to A: Lack of activity.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
34% identity, 79% coverage: 24:231/263 of query aligns to 18:230/375 of 2d62A
1g291 Malk (see paper)
33% identity, 78% coverage: 28:231/263 of query aligns to 19:227/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (≠ L76), K72 (= K77), K79 (≠ V84), D80 (≠ A85)
- binding pyrophosphate 2-: S38 (≠ N47), G39 (= G48), C40 (≠ S49), G41 (= G50), K42 (= K51), T43 (≠ S52), T44 (= T53)
Sites not aligning to the query:
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
35% identity, 78% coverage: 28:231/263 of query aligns to 22:216/353 of 1vciA
Sites not aligning to the query:
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
35% identity, 77% coverage: 30:231/263 of query aligns to 21:221/371 of P68187
- A85 (= A89) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ L118) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A126) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V129) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ Q131) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A139) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G152) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D173) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
Sites not aligning to the query:
- 228 R→C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 241 F→I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 267 W→G: Normal maltose transport but constitutive mal gene expression.
- 278 G→P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 282 S→L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 284 G→S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 302 G→D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 308 E→Q: Maltose transport is affected but retains ability to interact with MalT.
- 322 S→F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 340 G→A: Maltose transport is affected but retains ability to interact with MalT.
- 346 G→S: Normal maltose transport but constitutive mal gene expression.
- 355 F→Y: Maltose transport is affected but retains ability to interact with MalT.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
35% identity, 77% coverage: 30:231/263 of query aligns to 20:220/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (≠ N47), G38 (= G48), C39 (≠ S49), G40 (= G50), K41 (= K51), S42 (= S52), T43 (= T53), Q81 (= Q86), R128 (= R144), A132 (≠ S148), S134 (= S150), G136 (= G152), Q137 (≠ E153), E158 (= E174), H191 (= H203)
- binding magnesium ion: S42 (= S52), Q81 (= Q86)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
35% identity, 77% coverage: 30:231/263 of query aligns to 20:220/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G48), C39 (≠ S49), G40 (= G50), K41 (= K51), S42 (= S52), T43 (= T53), R128 (= R144), S134 (= S150), Q137 (≠ E153)
- binding beryllium trifluoride ion: S37 (≠ N47), G38 (= G48), K41 (= K51), Q81 (= Q86), S134 (= S150), G136 (= G152), H191 (= H203)
- binding magnesium ion: S42 (= S52), Q81 (= Q86)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
35% identity, 77% coverage: 30:231/263 of query aligns to 20:220/371 of 3puwA
- binding adenosine-5'-diphosphate: G38 (= G48), C39 (≠ S49), G40 (= G50), K41 (= K51), S42 (= S52), T43 (= T53), R128 (= R144), A132 (≠ S148), S134 (= S150), Q137 (≠ E153)
- binding tetrafluoroaluminate ion: S37 (≠ N47), G38 (= G48), K41 (= K51), Q81 (= Q86), S134 (= S150), G135 (= G151), G136 (= G152), E158 (= E174), H191 (= H203)
- binding magnesium ion: S42 (= S52), Q81 (= Q86)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
35% identity, 77% coverage: 30:231/263 of query aligns to 20:220/371 of 3puvA
- binding adenosine-5'-diphosphate: G38 (= G48), C39 (≠ S49), G40 (= G50), K41 (= K51), S42 (= S52), T43 (= T53), R128 (= R144), A132 (≠ S148), S134 (= S150), Q137 (≠ E153)
- binding magnesium ion: S42 (= S52), Q81 (= Q86)
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
35% identity, 77% coverage: 30:231/263 of query aligns to 18:218/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (≠ N47), G36 (= G48), C37 (≠ S49), G38 (= G50), K39 (= K51), S40 (= S52), T41 (= T53), R126 (= R144), A130 (≠ S148), S132 (= S150), G134 (= G152), Q135 (≠ E153)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
35% identity, 77% coverage: 30:231/263 of query aligns to 20:220/374 of 2awnB
Sites not aligning to the query:
5x40A Structure of a cbio dimer bound with amppcp (see paper)
36% identity, 84% coverage: 12:233/263 of query aligns to 4:229/280 of 5x40A
- binding phosphomethylphosphonic acid adenylate ester: F14 (≠ V22), V18 (vs. gap), A20 (≠ L27), N40 (= N47), G41 (= G48), G43 (= G50), K44 (= K51), S45 (= S52), T46 (= T53), Q88 (≠ E92), H139 (= H147), M140 (≠ S148), L141 (= L149), S142 (= S150), G144 (= G152), Q145 (≠ E153), Q166 (≠ E174), H198 (= H203)
- binding magnesium ion: S45 (= S52), Q88 (≠ E92)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
35% identity, 79% coverage: 24:231/263 of query aligns to 15:221/369 of P19566
- L86 (≠ V90) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P175) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D180) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
Sites not aligning to the query:
- 306 E→K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
7arlD Lolcde in complex with lipoprotein and adp (see paper)
35% identity, 76% coverage: 26:224/263 of query aligns to 20:222/222 of 7arlD
7mdyC Lolcde nucleotide-bound
35% identity, 76% coverage: 26:224/263 of query aligns to 20:222/226 of 7mdyC
- binding adp orthovanadate: G42 (= G48), S43 (= S49), G44 (= G50), K45 (= K51), S46 (= S52), T47 (= T53), Q91 (= Q93), H138 (= H147), E142 (≠ S148), S144 (= S150), G145 (= G151), G146 (= G152), E168 (= E174), N172 (≠ H178), H201 (= H203)
- binding magnesium ion: S46 (= S52), Q91 (= Q93)
Sites not aligning to the query:
P75957 Lipoprotein-releasing system ATP-binding protein LolD; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
35% identity, 76% coverage: 26:224/263 of query aligns to 23:225/233 of P75957
- G42 (= G45) mutation to D: Loss of lipoprotein release when overexpressed.
7v8iD Lolcd(e171q)e with bound amppnp in nanodiscs (see paper)
35% identity, 76% coverage: 26:224/263 of query aligns to 22:224/229 of 7v8iD
- binding phosphoaminophosphonic acid-adenylate ester: V23 (≠ L27), S43 (≠ N47), G44 (= G48), G46 (= G50), K47 (= K51), S48 (= S52), T49 (= T53), Q93 (= Q93), R137 (= R144), H140 (= H147), E144 (≠ S148), S146 (= S150), G148 (= G152), E149 (= E153), H203 (= H203)
- binding magnesium ion: S48 (= S52), Q93 (= Q93)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
35% identity, 78% coverage: 26:231/263 of query aligns to 31:235/378 of P69874
- F45 (≠ T40) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S49) mutation to T: Loss of ATPase activity and transport.
- L60 (= L55) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L71) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V136) mutation to M: Loss of ATPase activity and transport.
- D172 (= D173) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 26 C→A: Lower ATPase activity and transport efficiency.
- 27 F→L: Lower ATPase activity and transport efficiency.
- 276 C→A: Lower ATPase activity and transport efficiency.
- 297 mutation E->K,D: Lower ATPase activity and transport efficiency.; E→Q: Loss of ATPase activity and transport.
6b8bA E. Coli lptb in complex with adp and a novobiocin derivative (see paper)
30% identity, 88% coverage: 11:241/263 of query aligns to 1:233/233 of 6b8bA
- binding adenosine-5'-diphosphate: Y12 (≠ V22), R15 (≠ A25), V17 (≠ L27), G38 (= G48), G40 (= G50), K41 (= K51), T42 (≠ S52), T43 (= T53)
- binding (3s,5s,7s)-N-{7-[(3-O-carbamoyl-6-deoxy-5-methyl-4-O-methyl-beta-D-gulopyranosyl)oxy]-4-hydroxy-8-methyl-2-oxo-2H-1-benzopyran-3-yl}tricyclo[3.3.1.1~3,7~]decane-1-carboxamide: F89 (≠ L98), R90 (≠ D99), R91 (≠ A100)
6mhzA Vanadate trapped cryo-em structure of e.Coli lptb2fg transporter (see paper)
30% identity, 88% coverage: 11:241/263 of query aligns to 1:233/235 of 6mhzA
- binding adp orthovanadate: Y12 (≠ V22), N37 (= N47), G38 (= G48), G40 (= G50), K41 (= K51), T42 (≠ S52), T43 (= T53), Q84 (= Q93), S136 (= S148), S138 (= S150), G139 (= G151), G140 (= G152), E162 (= E174), G166 (≠ H178), H194 (= H203)
Query Sequence
>AO356_16420 FitnessBrowser__pseudo5_N2C3_1:AO356_16420
MNAVTSVIGESVLSCSALGFQVRDAELLHDIHLDIRRGETLGLVGPNGSGKSTLLKLLAG
VRAPSRGDIRLNNQPLKTLARRTVAQTLAVVEQQADTLDAISVFDAVALGRTPWLSALSP
WSNEDAAIVQQALWDVDAAHLKNRTWHSLSGGERQRVHIARALAQRPQILLLDEPTNHLD
IQHQLAILKVVQALPVTTVIALHDLNQALTCDRLAVLERGRLVALGKPLEVLTPQRLQDT
FGVHAHYLIDPFDGAQILRFRSV
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory